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Robert J. Tomko

Researcher at Florida State University

Publications -  37
Citations -  1725

Robert J. Tomko is an academic researcher from Florida State University. The author has contributed to research in topics: Proteasome & Protein degradation. The author has an hindex of 16, co-authored 34 publications receiving 1478 citations. Previous affiliations of Robert J. Tomko include University of Pittsburgh & Yale University.

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Molecular architecture and assembly of the eukaryotic proteasome.

TL;DR: Major new insights into chaperone-assisted proteasome assembly have also recently emerged, and a combination of cryo-electron microscopy, biochemical analysis, and crystal structure determination of several RP subunits has yielded a near-atomic-resolution view of much of the complex.
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microRNA-21 Negatively Regulates Cdc25A and Cell Cycle Progression in Colon Cancer Cells

TL;DR: In this article, the authors found that miR-21 is induced by serum starvation and DNA damage, negatively regulates G1-S transition, and participates in DNA damage-induced G2-M checkpoint through downregulation of Cdc25A.
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Multiple Assembly Chaperones Govern Biogenesis of the Proteasome Regulatory Particle Base

TL;DR: It is demonstrated that proteasomal RP biogenesis requires multiple, functionally overlapping chaperones and suggested a model in which subunits form specific subcomplexes that then assemble into the base.
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Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly.

TL;DR: The quaternary organization of the eukaryotic ATPase ring structure clarifies the functional overlap of specific RP assembly chaperones and led to identify a potential RP assembly intermediate that includes four ATPases and their cognate chaperone and the mechanism of RP action.
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Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating.

TL;DR: This work combines genetic and biochemical approaches with cryo-electron microscopy and integrative modeling to dissect the relationship between individual nucleotide binding events and proteasome conformational dynamics and reveals key elements of intersubunit communication within the proteasomes.